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G3V801

- NETR_RAT

UniProt

G3V801 - NETR_RAT

Protein

Neurotrypsin

Gene

Prss12

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 26 (01 Oct 2014)
      Sequence version 1 (16 Nov 2011)
      Previous versions | rss
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    Functioni

    Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei516 – 5172Reactive bond homologSequence Analysis
    Active sitei562 – 5621Charge relay systemBy similarity
    Active sitei612 – 6121Charge relay systemBy similarity
    Active sitei711 – 7111Charge relay systemBy similarity

    GO - Molecular functioni

    1. scavenger receptor activity Source: InterPro
    2. serine-type endopeptidase activity Source: Ensembl

    GO - Biological processi

    1. exocytosis Source: UniProtKB
    2. zymogen activation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.237.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neurotrypsin (EC:3.4.21.-)
    Alternative name(s):
    Serine protease 12
    Gene namesi
    Name:Prss12
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi69238. Prss12.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. cytoplasmic vesicle Source: Ensembl
    3. dendrite Source: Ensembl
    4. extracellular region Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB
    6. synaptic cleft Source: Ensembl
    7. terminal bouton Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 761740NeurotrypsinPRO_0000416843Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi85 ↔ 1571 Publication
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi101 ↔ 1411 Publication
    Disulfide bondi130 ↔ 1551 Publication
    Disulfide bondi191 ↔ 255By similarity
    Disulfide bondi204 ↔ 265By similarity
    Disulfide bondi235 ↔ 245By similarity
    Disulfide bondi298 ↔ 361By similarity
    Disulfide bondi311 ↔ 371By similarity
    Disulfide bondi341 ↔ 351By similarity
    Disulfide bondi411 ↔ 475By similarity
    Disulfide bondi424 ↔ 485By similarity
    Disulfide bondi455 ↔ 465By similarity
    Disulfide bondi505 ↔ 636Sequence Analysis
    Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi547 ↔ 563By similarity
    Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi651 ↔ 717By similarity
    Disulfide bondi680 ↔ 694By similarity
    Disulfide bondi707 ↔ 736By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000021116.

    Structurei

    Secondary structure

    1
    761
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi92 – 954
    Beta strandi98 – 1014
    Helixi104 – 1063
    Helixi119 – 1213
    Beta strandi131 – 1344
    Turni135 – 1373
    Beta strandi138 – 1447
    Beta strandi150 – 1545
    Beta strandi156 – 1583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2K4RNMR-A84-160[»]
    2K51NMR-A84-160[»]
    ProteinModelPortaliG3V801.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini85 – 15773KringlePROSITE-ProRule annotationAdd
    BLAST
    Domaini166 – 267102SRCR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini273 – 373101SRCR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini386 – 487102SRCR 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini517 – 760244Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni505 – 51612Zymogen activation regionBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 kringle domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 3 SRCR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Kringle, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00740000115025.
    HOGENOMiHOG000113767.
    KOiK09624.
    OMAiDDGWTDK.
    OrthoDBiEOG7RNK07.
    PhylomeDBiG3V801.
    TreeFamiTF329295.

    Family and domain databases

    Gene3Di2.40.20.10. 1 hit.
    3.10.250.10. 3 hits.
    InterProiIPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00051. Kringle. 1 hit.
    PF00530. SRCR. 3 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    PR00258. SPERACTRCPTR.
    SMARTiSM00130. KR. 1 hit.
    SM00202. SR. 3 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF56487. SSF56487. 3 hits.
    SSF57440. SSF57440. 1 hit.
    PROSITEiPS00021. KRINGLE_1. 1 hit.
    PS50070. KRINGLE_2. 1 hit.
    PS00420. SRCR_1. 3 hits.
    PS50287. SRCR_2. 3 hits.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    G3V801-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALARCVLAV ILGVLSEVAR ADPVLHSPLH RPHPSPPRSQ HAHYLPSSRR    50
    PPRTPRFPLP PRAPAAQRPQ LLSTRHTPPT ISRRCGAGEP WGNATNLGVP 100
    CLHWDEVPPF LERSPPASWA ELRGQPHNFC RSPGGAGRPW CFYRNAQGKV 150
    DWGYCDCGQG PALPVIRLVG GKSGHEGRVE LYHAGQWGTI CDDQWDDADA 200
    EVICRQLGLS GIAKAWHQAH FGEGSGPILL DEVRCTGNEL SIEQCPKSSW 250
    GEHNCGHKED AGVSCAPLTD GVIRLSGGKS VHEGRLEVYY RGQWGTVCDD 300
    GWTEMNTYVA CRLLGFKYGK QSSVNHFEGS SRPIWLDDVS CSGKEASFIQ 350
    CSRRQWGRHD CSHREDVGLT CYPDSDGHRL SPGFPIRLMD GENKREGRVE 400
    VFVSGQWGTI CDDGWTDKHA AVICRQLGYK GPARARTMAY FGEGKGPIHM 450
    DNVKCTGNEK ALADCVKQDI GRHNCRHSED AGVICDYYEK KTSGHGNKET 500
    LSSGCGLRLL HRRQKRIIGG NNSLRGAWPW QASLRLKSTH GDGRLLCGAT 550
    LLSSCWVLTA AHCFKRYGNN SRSYAVRVGD YHTLVPEEFE QEIGVQQIVI 600
    HRNYRPDSSD YDIALVRLQG SGEQCARLST HVLPACLPLW RERPQKTASN 650
    CHITGWGDTG RAYSRTLQQA AVPLLPKRFC KERYKGLFTG RMLCAGNLQE 700
    DNRVDSCQGD SGGPLMCEKP DETWVVYGVT SWGYGCGIKD TPGVYTRVPA 750
    FVPWIKSVTS L 761
    Length:761
    Mass (Da):84,220
    Last modified:November 16, 2011 - v1
    Checksum:i215EE73A3CE468EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1341G → D in CAC35028. 1 PublicationCurated
    Sequence conflicti404 – 4041S → N in CAC35028. 1 PublicationCurated
    Sequence conflicti515 – 5151K → T in CAC35028. 1 PublicationCurated
    Sequence conflicti565 – 5651K → T in CAC35028. 1 PublicationCurated
    Sequence conflicti588 – 5881E → G in CAC35028. 1 PublicationCurated
    Sequence conflicti592 – 5921E → D in CAC35028. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ311671 mRNA. Translation: CAC35028.2.
    CH473952 Genomic DNA. Translation: EDL82129.1.
    RefSeqiNP_445956.1. NM_053504.1.
    UniGeneiRn.86653.

    Genome annotation databases

    EnsembliENSRNOT00000021116; ENSRNOP00000021116; ENSRNOG00000015353.
    GeneIDi85266.
    KEGGirno:85266.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ311671 mRNA. Translation: CAC35028.2 .
    CH473952 Genomic DNA. Translation: EDL82129.1 .
    RefSeqi NP_445956.1. NM_053504.1.
    UniGenei Rn.86653.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2K4R NMR - A 84-160 [» ]
    2K51 NMR - A 84-160 [» ]
    ProteinModelPortali G3V801.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000021116.

    Protein family/group databases

    MEROPSi S01.237.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000021116 ; ENSRNOP00000021116 ; ENSRNOG00000015353 .
    GeneIDi 85266.
    KEGGi rno:85266.

    Organism-specific databases

    CTDi 8492.
    RGDi 69238. Prss12.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00740000115025.
    HOGENOMi HOG000113767.
    KOi K09624.
    OMAi DDGWTDK.
    OrthoDBi EOG7RNK07.
    PhylomeDBi G3V801.
    TreeFami TF329295.

    Miscellaneous databases

    NextBioi 617408.
    PROi G3V801.

    Family and domain databases

    Gene3Di 2.40.20.10. 1 hit.
    3.10.250.10. 3 hits.
    InterProi IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00051. Kringle. 1 hit.
    PF00530. SRCR. 3 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    PR00258. SPERACTRCPTR.
    SMARTi SM00130. KR. 1 hit.
    SM00202. SR. 3 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF56487. SSF56487. 3 hits.
    SSF57440. SSF57440. 1 hit.
    PROSITEi PS00021. KRINGLE_1. 1 hit.
    PS50070. KRINGLE_2. 1 hit.
    PS00420. SRCR_1. 3 hits.
    PS50287. SRCR_2. 3 hits.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of the cDNA encoding rat neurotrypsin."
      Hintsch G., Sonderegger P.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    4. Cited for: STRUCTURE BY NMR OF 84-160, PARTIAL PROTEIN SEQUENCE, DISULFIDE BOND, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiNETR_RAT
    AccessioniPrimary (citable) accession number: G3V801
    Secondary accession number(s): Q99JC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2012
    Last sequence update: November 16, 2011
    Last modified: October 1, 2014
    This is version 26 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3